Energy-level alignment is a crucial factor in the performance of thin-film devices, such as organic light-emitting diodes and photovoltaics. One way to adjust these energy levels is through chemical modification of the molecules involved. However, this approach may lead to unintended changes in the optical and/or electrical properties of the compound. An alternative method for energy-level adjustment at the interface is the use of self-assembling monolayers (SAMs). Initially, SAMs with passive spacers were employed, creating a surface dipole moment that altered the work function (WF) of the electrode. However, recent advancements have led to the synthesis of SAM molecules with active spacers. This development necessitates considering not only the modification of the electrode's WF but also the ionization energy (IE) of the molecule itself. To measure both the IE of SAM molecules and their impact on the electrode's WF, a relatively simple method is photo-electric emission spectroscopy. Solar cell performance parameters have a higher correlation coefficient with the ionization energy of SAM molecules with carbazole derivatives as spacers (up to 0.97) than the work function of the modified electrode (up to 0.88). Consequently, SAMs consisting of molecules with active spacers can be viewed as hole transport layers rather than interface layers.
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http://dx.doi.org/10.3390/molecules29091910 | DOI Listing |
Molecules
December 2024
College of Food Science & Technology, Huazhong Agricultural University, Wuhan 430070, China.
C-S lyase is a crucial enzyme responsible for the formation of sulfur-containing flavor compounds in . We investigated the involvement of C-S lyase in the synthesis of ergothioneine (EGT) in , a high-producing edible mushroom. Through experimental and computational approaches, we identified 2, a C-S lyase, as a key enzyme involved in EGT synthesis in .
View Article and Find Full Text PDFBioorg Med Chem
November 2024
Takeda Development Center Americas, Inc., 9625 Towne Centre Drive, San Diego, CA 92121, USA.
Interleukin-11 (IL-11), a member of the IL-6 cytokine family, has potential pro-inflammatory and pro-fibrotic roles in pulmonary, hepatic, cardiovascular, renal and intestinal disease pathogenesis, including oncogenesis. The potential for therapeutic intervention in these disease spaces has therefore made the IL-11 signaling axis an attractive target in drug discovery, and antibody inhibitors of IL-11 signaling are currently under evaluation in Phase I/II clinical trials. While lower molecular weight small molecule and peptide inhibitors may offer the potential for improved tissue penetration, developability and manufacturing cost compared with a protein therapeutic, reports of such chemical matter in the literature are limited.
View Article and Find Full Text PDFACS Appl Mater Interfaces
December 2024
Department of Applied Chemistry and Institute of Molecular Science, National Yang Ming Chiao Tung University, 1001 Ta-Hseuh Road, Hsinchu 300093, Taiwan.
Three new bithiophene imide (BTI)-based organic small molecules, (), (), and (), with varied alkyl side chains, were developed and employed as self-assembled monolayers (SAMs) applied to NiOx films in tin perovskite solar cells (TPSCs). The NiOx layer has the effect of modifying the hydrophilicity and the surface roughness of ITO for SAM to uniformly deposit on it. The side chains of the SAM molecules play a vital role in the formation of a high-quality perovskite layer in TPSCs.
View Article and Find Full Text PDFScience
December 2024
Department of Immunology, University of Washington, Seattle, WA.
Antiviral signaling downstream of RIG-I-like receptors (RLRs) proceeds through a multi-protein complex organized around the adaptor protein mitochondrial antiviral signaling protein (MAVS). Protein complex function can be modulated by RNA molecules that provide allosteric regulation or act as molecular guides or scaffolds. We hypothesized that RNA plays a role in organizing MAVS signaling platforms.
View Article and Find Full Text PDFCell Death Dis
December 2024
Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.
The concept of Targeted Protein Degradation (TPD) has been introduced as an attractive alternative to the development of classical inhibitors. TPD can extend the range of proteins that can be pharmacologically targeted beyond the classical targets for small molecule inhibitors, as a binding pocket is required but its occupancy does not need to lead to inhibition. The method is based on either small molecules that simultaneously bind to a protein of interest and to a cellular E3 ligase and bring them in close proximity (molecular glue) or a bi-functional molecule synthesized from the chemical linkage of a target protein-specific small molecule and one that binds to an E3 ligase (Proteolysis Targeting Chimeras (PROTAC)).
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